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Protein and Amino Acids, 1999

Pp. 19-75. Washington, D.C.

National Academy Press

1
Committee Overview

INTRODUCTION

Proteins form the major constituents of muscle, catalyze virtually all chemical reactions in the body, regulate gene expression, and comprise the major structural elements of all cells. Individual amino acids, the components of proteins, also serve as neurotransmitters, hormones, and modulators of various physiological processes. Every aspect of physiology involves proteins. According to Bier (see Chapter 5), credit for the name "protein" is given to the Dutch chemist Gerardus Johannes Mulder, who wrote an article in French that was published in a Dutch journal on July 30, 1838. In this article, he asserted that this material was the essential general principle of all animal body constituents and defined it by the Greek word proteus (which he translated to the Latin, primarius, meaning primary). Mulder appears to have taken this word directly from a letter sent to him by the Swedish chemist Jacques Bursailleus on July 10, 1838, in which the name protein had been suggested. Aside from the amazing fact of a Dutch chemist borrowing n Latin word from a Swedish



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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Protein and Amino Acids, 1999 Pp. 19-75. Washington, D.C. National Academy Press 1 Committee Overview INTRODUCTION Proteins form the major constituents of muscle, catalyze virtually all chemical reactions in the body, regulate gene expression, and comprise the major structural elements of all cells. Individual amino acids, the components of proteins, also serve as neurotransmitters, hormones, and modulators of various physiological processes. Every aspect of physiology involves proteins. According to Bier (see Chapter 5), credit for the name "protein" is given to the Dutch chemist Gerardus Johannes Mulder, who wrote an article in French that was published in a Dutch journal on July 30, 1838. In this article, he asserted that this material was the essential general principle of all animal body constituents and defined it by the Greek word proteus (which he translated to the Latin, primarius, meaning primary). Mulder appears to have taken this word directly from a letter sent to him by the Swedish chemist Jacques Bursailleus on July 10, 1838, in which the name protein had been suggested. Aside from the amazing fact of a Dutch chemist borrowing n Latin word from a Swedish

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance chemist, which he defined in Greek in an article written in French for a Dutch journal, the entire sequence of events appears to have occurred in a period of 20 days, demonstrating the efficiency of both mail service and scientific publication in those days. The relationship between dietary protein and bodily protein metabolism is a major focus of research today. Many questions remain regarding the validity of methods for assessing protein balance; thus, the question of how best to assess dietary protein requirements remains unanswered. In addition, the influence of genetics, hormones, physical activity, infectious processes, and environmental stresses on protein metabolism and protein requirements continues to be explored. Another major focus of research that is of great interest is the role of dietary protein and amine acids in modulating physiological function, as measured for example by physical and mental performance. The possibility that protein or individual amine acids in quantities that exceed those required to maintain protein balance may have the potential to contribute to performance optimization is of great interest. THE ARMY'S INTEREST IN DIETARY PROTEIN AND PROTEIN BALANCE Because of the unique demands placed on soldiers in combat, the military is particularly concerned about the role that dietary protein may play in controlling muscle mass and strength; response to injury, infection, and environmental stress; and cognitive performance. As described in Chapter 3 by Karl Friedl, the longer, more isolated deployments and maneuvers that are becoming more commonplace may limit access to rations. The nutritional studies of Ranger trainees conducted by the U.S. Army Research Institute of Environmental Medicine (USARIEM) (IOM, 1992, 1993b) identified losses of up to 30 percent in lean body mass (including organs, such as the liver, plasma, and proteins) after 3 weeks of limited food intake and high energy expenditure. Although increased energy intake offset these losses somewhat, they were still significant, suggesting the need for additional energy, protein, or both. In these studies, the observed decrease in lean body mass was accompanied by changes in serum levels of several hormones including testosterone, insulin-like growth factor I (IGF-I), and triiodothyronine (T3) (Friedl, 1997; Nindl et al., 1997), the significance of which is unclear. Because the administration of these hormones is known to stimulate protein synthesis under some conditions, the Army maintains considerable interest in exploring their potential both to ameliorate the losses in lean body mass sustained by troops under conditions of extreme negative energy balance and to stimulate an increase in muscle mass and physical performance. In contrast to the limited intakes of protein and energy measured in the Ranger studies, a more recent study, in which soldiers subsisted on the field ration known as Meals, Ready to Eat (MREs) for 30 days, showed

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance average energy intakes of 2500 kcal/d and protein intakes of 103 g/d (Thomas et al., 1995), raising questions about the optimum protein-to-energy ratio for performance and health. As the typical battlefield scenario becomes more automated, soldiers must attend to increasing numbers of signals in the face of increasing amounts and sources of noise, with increasingly dangerous consequences for failure. Thus, the possibility that cognitive performance may depend on diet and that performance optimization may be achievable through dietary modifications such as amino acid supplements is of considerable interest to the military. A 1994 report by the Committee on Military Nutrition Research (CMNR), entitled Food Components to Enhance Performance, briefly considered the influence of protein and amino acids (and all other dietary components) on physical and cognitive performance and response to stress (IOM, 1994). Data were presented on the effect of protein-to-carbohydrate ratio on mental alertness, the effect of physical activity on protein requirements, and the influence of branched-chain amino acids, tyrosine, and tryptophan in pharmacological amounts on cognitive function. The report concluded that the potential ability of tyrosine supplements to sustain alertness and cognitive performance in the face of environmental stress merited further investigation. Finally, the risk of injury and infection faced by soldiers in the field is extremely high. At the same time, conditions of sleep and food deprivation, environmental extremes, and heightened emotional stress all exert a negative impact on the immune system. The CMNR report Military Strategies for Sustainment of Nutrition and Immune Function in the Field (IOM, 1999), considered the effects of diet, including protein and individual amino acids such as glutamine, on immune response and concluded that although the role of energy intake in immune function is probably more significant than that of protein, individual amino acids such as glutamine and arginine appear to play crucial roles in modulating immune function. The effects of these amino acids are considered in greater detail in this report. ESTIMATION OF PROTEIN REQUIREMENTS Current estimates of protein requirements for mature humans and the methods used to assess these requirements are being scrutinized by the research community and are a source of considerable disagreement. Protein Metabolism The requirement for protein arises from growth, from the need to replace obligatory losses, and from the need to respond to environmental stimuli. The

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance FIGURE 1-1 Pathways of protein turnover. Source: Young and Marchini, 1990. breakdown products of protein—amino acids—enter the free amino acid pool of the body (distributed among body fluids and tissues) from four sources: (1) dietary proteins; (2) so-called dispensable (nonessential) amino acids, which can be synthesized in the body; (3) breakdown products of body protein (particularly skeletal muscle, the largest tissue in the body and the site of protein storage); and (4) the products of recycling by intestinal microbes (Figure 1-1). In mature humans, a homeostatic mechanism maintains the balance between tissue protein synthesis and breakdown by drawing on the free amino acid pool. Methods for Assessment of Protein Requirements Because the majority of nitrogen in the body is associated with protein and amino acids, nitrogen has been used as a marker for assessing whole-body and tissue protein flux and status. The traditional method for assessing whole-body protein metabolism is nitrogen balance, where nitrogen (N) intake and output (in feces, sweat, and urine, as well as other miscellaneous sources) are measured and the difference [Nbal=(Nin = Nout)] is expressed in grams of nitrogen per day (g N/d). Total body protein loss or retention is then calculated using the conversion factor of 6.25 g N/g protein (Munro and Crim, 1994). A state of positive nitrogen balance exists when the total nitrogen output is less than the total nitrogen ingested. Positive nitrogen balance requires adequate protein and energy intake plus a stimulus for synthesis. A state of positive nitrogen balance (an anabolic state) exists for the synthesis of new tissues during the growth observed in childhood, adolescence, and pregnancy. When dietary protein or energy intake is inadequate or an individual experiences an acute-

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance phase response, nitrogen excretion exceeds nitrogen intake and a state of negative nitrogen balance exists (net protein catabolism). When dietary protein is adequate or more than adequate and energy intake matches energy output, a state of nitrogen equilibrium exists (Nin = Nout for any intake above the required level). A state of nitrogen equilibrium is required to maintain total body protein mass. Altering protein or energy intake or physical activity may alter nitrogen balance. Despite the usefulness of nitrogen balance assessment in estimating the adequacy of protein intake, there are significant limitations to its use, including overestimation of nitrogen intake and incomplete collections of urine, feces, or sweat, which result in an underestimation of nitrogen output. The net outcome is an overestimate of nitrogen retention and of the body's ability to adapt to inadequate protein intakes; these overestimates limit the ability of the nitrogen balance technique to assess nitrogen requirement. The limitations of nitrogen balance assessment are discussed further below and by Millward and Young in Chapters 9 and 10, respectively. In the mid-1940s, stable isotopes of hydrogen (2H) and nitrogen (15 N), were made available for use in biomedical research. However, the mass spectrometry technology that would use these isotopes for rapid analysis of biological specimens was not widely available until the late 1970s. With the improvement of this technology and the widespread availability of stable isotope-labeled metabolites, amino acid kinetic studies have come to augment nitrogen balance in examining the effects of dietary protein, energy, and physical activity on overall protein metabolism. Amino acids labeled with stable isotopes of hydrogen (2H), nitrogen (15N), and carbon (13C) have been administered orally and intravenously. With the use of the primed continuous infusion technique, amino acid turnover can be studied in subjects of all ages under many physiological conditions (Munro and Crim, 1994). The calculation of amino acid flux (Q) is based on the following assumptions: (1) the body's flee amino acid pool is a homogeneous mixture that can be sampled from the plasma pool; (2) the only sources of the target amino acids entering the body pool are dietary protein (I) and intracellular protein breakdown (B); and (3) amino acid removal from this pool occurs by irreversible oxidation (E) or synthesis into protein (Z). In reality, a large quantity of recycled amino acids is derived daily from the breakdown of body proteins. In addition to the sizable turnover of blood cells, mucosal cells of gastric and intestinal villi are continuously moved toward villus tips where they slough off and undergo digestion; released free amino acids are then reabsorbed into the plasma pool (Munro and Crim, 1994). Thus, the equation Q = B + I = E + Z describes the steady-state relationship in which the total entry of amino acids into the free amino acid pool (B + I) is equal to the total exit of amino acids from the free amino acid pool (E + Z). Rates of protein synthesis and protein breakdown can be calculated from this equation (Picou and Taylor-

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Roberts, 1969). At isotopic steady state, total amine acid turnover (Q) is measured, and the rate of protein breakdown can be calculated knowing the rate of amine acid intake. Likewise, the rate of protein synthesis can be calculated when the rate of amine acid disappearance is known. If a 13C-labeled amine acid is used, oxidation can be measured from 13CO2 excretion rates. Because of its unique role as an amine acid that is oxidized in skeletal muscle and not converted to a tricarboxylic acid (TCA) cycle intermediate, leucine (in the 13C form) has been the amine acid of choice for many amine acid kinetic studies. However, due to its unique metabolism, it may not be representative of the entire pool of amine acids. Glycine labeled with 15N has also been used extensively to study protein synthesis and breakdown because it has the advantage of ubiquitous utilization. FAO/WHO/UNU Requirements and RDAs: Current Estimates of Average Protein Intake Estimations of protein and amine acid requirements are currently based on nitrogen balance studies. The 1985 report of the Food and Agriculture Organization (FAO), World Health Organization (WHO), and United Nations University (UNU) proposed a protein requirement of 0.625 g per kilogram of body weight per day (g/kg BW/d) for egg or beef protein and a ''safe" level of 0.75 g/kg BW/d for mixed protein if the protein is as digestible as egg or beef (FAO/WHO/UNU, 1985). The current recommended dietary allowance (RDA) for protein in the U.S. diet (which is derived by adding two standard deviations to the estimated requirement) is 0.8 g/kg BW/d for adult men and women (Table 1-1) (NRC, 1989). Also based on nitrogen balance data, the recommendation for total essential or indispensable amine acids (IAAs) as a percentage of protein intake is 43 percent for infants and 11 percent for adults (FAO/WHO/UNU, 1985). Essential (indispensable) and nonessential (dispensable) amine acids are traditionally distinguished on a nutritional basis because essential amine acids cannot be synthesized by the body and must be part of the diet to permit growth or to maintain nitrogen balance, whereas nonessential amine acids can be synthesized by the body. Metabolically, however, the distinctions are less clear because a number of essential amine acids can be formed by transamination (at least in laboratory animals). By this criterion, only the amine acids lysine and threonine appear not to be synthesized by transamination and are therefore indispensable (as discussed further below, the concentrations of these two amine acids in cereal proteins are so low as to limit their ability to sustain growth). By this same argument, glutamic acid and serine are the only truly dispensable amine acids because they can be synthesized by reductive amination of ketoacids. A

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance TABLE 1-1 Recommended Dietary Allowances for Protein Age (years) or Condition Weight (kg) RDA g/d RDAg/kg BW/d Males 19-24 72 58 0.8 25-50 79 63 0.8 51+ 77 63 0.8 Females 19-24 58 46 0.8 25-50 63 50 0.8 51+ 65 50 0.8 Pregnant   60   Lactating (first 6 months)   65   Lactating (second 6 months)   62     SOURCE: Adapted from NRC (1989). third class—the conditionally essential amino acids—is synthesized from other amino acids. However, this synthesis is confined to particular organs and may be limited by certain physiological factors such as age or disease state (Reeds and Becket, 1996). As knowledge increases and techniques improve, the distinction between essential and nonessential amino acids becomes less clear. Adding to this lack of clarity are observations such as the one by Stucky and Harper (1962), who found that if rats were fed a diet adequate in nitrogen but lacking in nonessential amino acids, the growth rate of the animals was significantly decreased. Importance of the Debate over Indispensable Amino Acid Requirements Although consensus exists at present for the adult protein requirement this is not the case for the adult requirement of indispensable amino acids. Since the 1985 FAO/WHO/UNU report, Young and coworkers have presented data that contradict the findings of the report; based on these data, Young suggests that the adult requirement for total IAAs is 31 percent of the protein requirement, or about three times the FAO/WHO/UNU estimate (McLarney et al., 1996; Young, 1987, 1994; Young and El-Khoury, 1995a; Young and Marchini, 1990; Young et al., 1989; see also Chapter 10). This contention of the group at Massachusetts Institute of Technology (MIT) for higher indispensable amino acid needs has been countered by Millward and colleagues (Millward, 1994; Millward and Rivers, 1988, 1989; see also Chapter 9), who find significant methodological problems in the studies of Young and coworkers. This debate is important, because it influences whether or not protein quality is an issue to be considered

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance in setting protein requirements. Protein quality, a measure of the efficiency with which dietary protein is utilized, can be assessed by comparison of the amine acid profile of a given protein to various amine acid scoring patterns such those developed by the FAO/WHO for various age groups. If the requirement for IAAs is low (as proposed by FAO/WHO and Millward), the pattern is easily matched by most proteins, and protein quality ceases to be an issue in setting protein requirements for adults. However, if the FAO estimates are incorrect and indispensable amine acids are required in the higher amounts proposed by Young, individual protein sources may duplicate the scoring patterns poorly, and protein quality may then become a significant determinant of protein requirements. Argument for Higher Indispensable Amine Acid Requirements Young has based his argument for higher indispensable amine acid requirements on two related measures: the obligatory oxidative losses of these amine acids and the calculated obligatory losses based on daily nitrogen loss. In the latter calculation, Young assumes that the efficiency of dietary protein use is about 70 percent and that the lost protein has the composition of mixed body protein. Indispensable amine acid requirements calculated in these two ways (the MIT pattern) are approximately the same. In 1991, an expert panel of FAO/WHO also agreed that the IAA needs for adults are greater than those in the 1985 report and proposed that the amine acid pattern for preschool children (FAO/WHO, 1991), a pattern similar to the MIT pattern, be recommended for adults. Young argues that protein and indispensable amine acid intakes have to be high enough to provide sufficient flux for optimum "metabolic control." This concept proposes that a high flux rate of amine acids or other substrates provides a kinetic basis for a sensitive control mechanism to ensure adequate provision of metabolic intermediates. In the case of protein, these important intermediates would be amine acids such as glutamine, tyrosine, and tryptophan, which have important physiological roles to play independent of their incorporation into protein. To prove their point, Young and colleagues carried out a long-term study to compare the effects of the FAO (FAO/WHO/UNU, 1985), MIT, and egg patterns of indispensable amine acids on amine acid balance in healthy young adults (Marchini et al., 1993). After a week on the egg pattern (high in IAAs), 20 young men were placed on diets resembling either the FAO, the MIT, or the egg pattern for three weeks. Based on a negative leucine balance while the subjects were on the FAO (compared with the MIT) pattern and changes in serum amine acid profiles, Marchini et al. (1993) concluded that the FAO pattern is not capable of maintaining amine acid homeostasis. Since the 1991 FAO/WHO meeting, several groups have reevaluated the existing data and concluded that the original FAO recommendations were likely

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance to be underestimates but stopped short of endorsing the MIT pattern (Fuller and Garlick, 1994; Waterlow, 1996). In 1994, an expert panel met to consider the issue. After the meeting, the panel recommended that the entire question of how amino acid requirements are determined be reexamined but that, in the interim, the MIT pattern be accepted (Clugston et al., 1996). However, as subsequently pointed out by Millward and Waterlow (1996), this recommendation was not the consensus of the attendees but was inserted during postmeeting editing. Argument Against Higher Indispensable Amino Acid Requirements Millward and colleagues have challenged Young's data point by point (Millward, 1994; Millward and Rivers, 1988, 1989; see also Chapter 9). They suggest first that Young's stable isotope amino acid oxidation data, derived from stable isotope-labeled amino acid infusion studies, are flawed for two reasons. First, the amount of tracer used in the infusion studies is itself high enough to influence the oxidation of the amino acid and thus the balance determined. Second, the enrichment of the amino acid precursors being oxidized is not accurately measured, a critical issue in the interpretation of stable isotope research. Next, Millward argues that there is no valid basis for assuming that the obligatory amino acid losses (as calculated from obligatory nitrogen loss) resemble the pattern of body protein, because some of the amino acids released during normal turnover are known to be preferentially recycled (lysine and threonine). In addition, he believes that the metabolic demand for IAAs is determined not by the need for high flux rates, but by the obligatory losses and the relative ability of the body to adapt on a diurnal basis to varying levels of these amino acids in the diet (he notes that digestive enzymes secreted in response to a meal can, over the short run, assist in meeting the indispensable amino acid needs by breaking down themselves). Finally, Millward points out that in the longer-term study mentioned above (Marchini et al., 1993), nitrogen balance did not differ significantly between the MIT and the FAO patterns; this finding suggests that both patterns support overall body protein economy. The Rebuttal Young agrees with Millward that there are inherent difficulties in defining requirements for indispensable amino acids. The two most serious and difficult-to-resolve problems are (1) accounting for the mass of stable isotope infused, which is large enough to affect nitrogen balance, and (2) determining the true precursor enrichment rate of the amino acid being infused and under study. On the first point, the agreement between IAA requirements calculated from oxidation rates and from nitrogen balance leads Young to conclude that the

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance mass of stable isotope infused does not "profoundly" affect the calculation of amine acid oxidation rates. He agrees, however, that this issue deserves more attention. On the question of true precursor amine acid enrichments in the stable isotope experiments, Young points out that this is a problem primarily for lysine since measurements in experiments with branched-chain amine acids are made from keto acids derived intracellularly from the infused amine acid. Studies using L-[l-13C]phenylalanine as an indicator amine acid for determining the lysine requirement have yielded a requirement of 40 mg/kg BW/d (Duncan et al.; 1996, Zello et al., 1993), an estimate close to Young's own tentative new requirement for lysine (50 mg/kg BW/d). In this technique, the indicator amine acid (labeled phenylalanine) is infused at graded levels of lysine intake, and the "breakpoint" in 13CO2 excretion is measured, under the assumption that the uptake of phenylalanine into protein will be sharply decreased and its oxidation sharply increased at the point where lysine intake becomes inadequate. Young's definition of the maintenance amine acid pattern for adults is generally similar to the amine acid pattern in body protein, except for lysine, threonine, and methionine, whose patterns were derived more from the results of his tracer studies. Young agrees that the body has significant ability to conserve lysine under conditions of inadequate intake. His calculations suggest that the lysine requirement is 30 percent lower than that found in mixed body protein, due to lysine conservation that results from diurnal cycling. Resolution of the Debate The practical implications of the debate between Young and Millward revolve primarily around lysine: the lysine content of cereal proteins is limiting for growth. If Millward is correct, then all dietary proteins, whether plant or animal, contain enough lysine and other amine acids to support adequate protein nutriture of adults if consumed in amounts that meet the protein requirement (although some military personnel in the 18-22-year age group are still growing, a factor that might influence the requirement for some amine acids). Millward has shown that wheat protein, a protein that is particularly low in lysine, is well utilized in adults in the postprandial period, even when net protein synthesis occurs. He suggests that the low level of lysine in this protein is supplemented by the tissue free amine acid pools. However, older data from Longenecker (Longenecker, 1961, 1963; Longenecker and Hause, 1959, 1961) show that the ingestion of wheat protein by dogs or humans may result in decreased plasma lysine levels accompanied by increased levels of other indispensable amine acids. Such data support the contention that a postprandial breakdown of body protein may supply the indispensable amine acids necessary for synthesis. However, under such circumstances, other IAAs may be used less efficiently for protein synthesis when lysine is limiting in the protein consumed,

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance which supports Young's belief that the indispensable amino acid requirement is higher than currently recommended. Thus, the controversy over requirements for IAAs is still unresolved. The implications of this debate for the current state of knowledge of protein and amino acid requirements for the military depend in part on the current intake of dietary protein and amino acids by military personnel and in part on other factors influencing protein requirements in these individuals, as discussed below. STRESSORS THAT INFLUENCE PROTEIN REQUIREMENTS As discussed by Friedl in Chapter 3, the stressors encountered most frequently by military personnel are high levels of physical activity with Or without energy restriction; illness, injury, and infection; and environmental extremes. Although each of these stressors may somehow influence protein metabolism and protein requirements directly, they also produce changes in hormonal status that can influence protein metabolism as well. The impact of each of these factors on protein metabolism and requirements has been the subject of intense investigation in the civilian research community. A brief summary of relevant findings is presented here. Physical Activity and Energy Restriction The question of whether individuals who routinely engage in intensely physical occupational or athletic activities have increased requirements for dietary protein appears to have arisen from the observations that during exercise, muscle protein is utilized for fuel and that exercise can lead to an increase in muscle mass. However, whether protein requirements are in fact increased by physical activity is unclear and a subject of intense controversy. In Chapter 11, Rennie reviews the role of protein and its breakdown products, amino acids, in exercising muscle and discusses changes in protein metabolism induced by energy deficit. Exercise and Amino Acid Catabolism A major function of amino acid breakdown in muscle during periods of exercise is to supply tricarboxylic acid intermediates (anaplerosis) so that the oxidation of acetyl coenzyme A (CoA) can proceed at rates appropriate to the energy needs of the contractile apparatus. The exercise-induced increase in muscle alanine production may be a marker for this process. Specifically, glutamate can react with pyruvate, via the action of alanine-aminotransferase, to produce alanine and α-ketoglutarate. The latter then feeds into the TCA cycle,

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Davis, J.M., S.P. Bailey, J.A. Woods, F.J. Galiano, M.T. Hamilton, and W.P. Bartoli. 1992. Effects of carbohydrate feedings on plasma free tryptophan and branched chain amine acids during prolonged cycling. Eur. J. Appl. Physiol. 65:513-519. Deijen, J.B., and J.F. Orlebeke. 1994. Effect of tyrosine on cognitive function and blood pressure under stress. Brain Res. Bull. 33:319-323. Delgado, P.L., D.S. Charney, L.H. Price, G.K. Aghajanian, H. Landis, and G.R. Heninger. 1990. Serotonin function and the mechanism of antidepressant action. Reversal of antidepressant-induced remission by rapid depletion of plasma tryptophan.. Arch. Gen. Psychiatry 47:411-418. Duncan, A.M., R.O. Ball, and P.B. Pencharz. 1996. Lysine requirement of adult males is not affected by decreasing dietary protein intake. Am. J. Clin. Nutr. 64:718-725. Edwards, J.S.A., E.W. Askew, N. King, C.S. Fulco, R.W. Hoyt, and J.P. DeLany. 1991. An assessment of the nutritional intake and energy expenditure of unacclimatized U.S. Army soldiers living and working at high altitude. Technical Report No. T10-91. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Elahi, D., M. McAloon-Dyke, N.K. Fukagawa, A.L. Sclater, G.A. Wong, R.P. Shannon, K.L. Minaker, J.M. Miles, A.H. Rubenstein, and C.J. Vandepol. 1993. Effects of recombinant human IGF-I on glucose and leucine kinetics in men. Am. J. Physiol. 265:E831-E838. FASEB/LSRO. 1992. Safety of amine acids used as dietary supplements. Center for Food Safety and Applied Nutrition. FDA Contract No. 223-88-2124, Task No. 8. FAO/WHO (Food and Agriculture Organization of the United Nations/World Health Organization). 1991. Protein Quality Evaluation. Report of a Joint FAO/WHO Expert Consultation. FAO Food and Nutrition Paper 51. Rome: FAO. FAO/WHO/UNU ((Food and Agriculture Organization of the United Nations/World Health Organization)/United Nations University). 1985. Energy and protein requirements. Report of a joint expert consultation. World Health Organization Technical Report Series No. 724. Geneva: World Health Organization. Fernstrom, J.D. 1990. Aromatic amine acids and monoamine synthesis in the central nervous system: Influence of the diet. J. Nutr. Biochem. 1:508-517. Fernstrom, J.D. 1994. Stress and monoamine neurons in the brain. Pp. 161-175 in Food Components to Enhance Performance, B.M. Marriott, ed. Institute of Medicine. Washington, D.C.: National Academy Press. Fernstrom, J.D., and M.J. Hirsch. 1975. Rapid repletion of brain serotonin in malnourished, corn-fed rats following L-tryptophan injection. Life Sciences 17:455-464. Fernstrom, J.D., and L.D. Lytle. 1976. Corn malnutrition, brain serotonin, and behavior. Nutr. Rev. 34:257-262. Fernstrom, J.D., and R.J. Wurtman. 1971. Brain serotonin content: Physiological dependence on plasma tryptophan levels. Science 173:149-152. Feskanich, D., W.C. Willett, M.J. Stampfer, and G.A. Colditz. 1996. Protein consumption and bone fractures in women. Am. J. Epidemiol. 143:472-479. Fielding, R.A., C.N. Meredith, K.P. O'Reilly, W.R. Fontera, J.G. Cannon and N.J. Evans. 1991. Enhanced protein breakdown after eccentric exercise in young and older men. J. Appl. Physiol. 11:674-679. Frieder, B., and V.E. Grimm. 1984. Prenatal monosodium glutamate (MSG) treatment given through the mother's diet causes behavioral deficits in rat offspring. Int. J. Neurosci. 23(2):117-126. Friedl, K.E. 1997. Variability of fat and lean tissue loss during physical exertion with energy deficit . Pp. 431-450 in Physiology, Stress, and Malnutrition: Functional Correlates, Nutritional Intervention, J.M. Kinney and H.N. Tucker, eds. Philadelphia: Lippincott-Raven Publishers.

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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Friedman, M. 1991. Formation, nutritional value, and safety of d-amino acids. Pp. 447-492 in Nutritional and Toxicological Consequences of Food Processing. New York: Plenum Press. Fryburg, D.A. 1994. Insulin-like growth factor I exerts growth hormone and insulin-like actions on human muscle protein metabolism. Am. J. Physiol. 267:E331-E336. Fryburg, D.A. 1996. NG-monomethyl-L-arginine inhibits the blood flow but not the insulin-like response of forearm muscle to IGF- I: possible role of nitric oxide in muscle protein synthesis. J. Clin. Invest. 97:1319-1328. Fryburg, D.A., and E.J. Barrett. 1993. Growth hormone acutely stimulates skeletal muscle but not whole-body protein synthesis in humans. Metabolism 42:1223-1227. Fryburg, D.A., R.A. Gelfand, and E.J. Barrett. 1991. Growth hormone acutely stimulates forearm protein synthesis in normal subjects. Am. J. Physiol. 260:E499-E504 Fryburg, D.A., L.A. Jahn, S.A. Hill, D.M. Oliveras, and E.J. Barrett. 1995. Insulin and insulin-like growth factor I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms. J. Clin. Invest. 96:1722-1729. Fuller, M.F., and P.J. Garlick. 1994. Human amino acid requirements: Can the controversy be resolved? Ann. Rev. Nutr. 14:217-241. Funk, D.N., B. Worthington-Roberts, and A. Fantel. 1991. Impact of supplemental lysine or tryptophan on pregnancy course and outcomes in rats. Nutr. Res. 11:501-512. Gallagher, D., D. Belmonte, P. Deurenberg, Z. Wang, N. Krasnow, F.X. Pi-Sunyer, S.B. Heymsfield. 1998. Organ-tissue mass measurement allows modeling of REE and metabolically active tissue mass. Am. J. Physiol. 275:E249-E258. Gontzea, I., P. Sutzescu, and S. Dumitrache. 1975. The influence of adaptation to physical effort on nitrogen balance in man. Nutrition Reports International 22:231-236. Gore, D.C., D. Honeycutt, F. Jahoor, R.R. Wolfe, and D.N. Herndon. 1991. Effect of exogenous growth hormone on whole-body and isolated-limb protein kinetics in burned patients. Arch. Surg. 126:38-43. Griffiths, R.D., C. Jones, and T.E.A. Palmer. 1997. Six-month outcome of critically ill patients given glutamine-supplemented parenteral nutrition. Nutrition 13(4):295-302. Hartmann, E., and D. Greenwald. 1984. Tryptophan and human sleep: An analysis of 43 studies. Pp. 297-304 in Progress in Tryptophan and Serotonin Research, H.G. Schlossberger, W. Kochen, B. Linzen, and H. Steinhart, eds. Berlin: Walter de Gruyter. Hegsted, M., and H.M. Linkswiler. 1981. Long-term effects of level of protein intake on calcium metabolism in young adult women. J. Nutr. 111:244-251. Hegsted, M., S.A. Schuette, M.B. Zemel, and H.M. Linkswiler. 1981. Urinary calcium and calcium balance in young men as affected by level of protein and phosphorus intake. J. Nutr. 111:553-562. Hertzman, P.A., W.L. Blevins, J. Mayer, B. Greenfield, M. Ting, and G.J. Gleich. 1990. Association of the eosinophilia-myalgia syndrome with the ingestion of tryptophan. N. Engl. J. Med. 322:869-873. Heymsfield, S.B., D. Gallagher, M. Visser, C. Nuñez, and Z-M. Wang. 1995. Measurement of skeletal muscle: Laboratory and epidemiological methods. J. Gerontol. 50A:23-29. Heymsfield, S.B., R. Ross, Z. Wang, D. Frager. 1997. Imaging Techniques of Body Composition: Advantages of Measurement and New Uses. Pp. 127-150 in Emerging Technologies for Nutrition Research, S.J. Carlson-Newberry and R.B. Costello, eds. Institute of Medicine. Washington, DC: National Academy Press. Hirsch, E., W. Johnson, P. Dunne, C. Shaw, N. Hotson, W. Tharion, H. Lieberman, R. Hoyt, and D. Dacumos. In press. The effects of diet composition on food intake, food selection, and water balance in a hot environment. Technical Report. Natick, Mass.: Natick Research, Development and Engineering Center.

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Hoyt, R.W., and A. Honig. 1996. Body fluid and energy metabolism at high altitude. Pp. 1277-1289 in Handbook of Physiology, Section 4: Environmental Physiology, C.M. Blatteis and M.J. Fregly, eds. New York: Oxford University Press for the American Physiological Society. Huether, G., F. Thomke, and L. Adler. 1992. Administration of tryptophan-enriched diets to pregnant rats retards the development of the serotonergic system in their offspring. Brain Res. Dev. Brain Res. 68(2):175-181. IOM (Institute of Medicine). 1992. A Nutritional Assessment of U.S. Army Ranger Training Class 11/91. March 23. Washington, D.C. IOM. 1993b. Review of the Results of Nutritional Intervention, U.S. Army Ranger Training Class 11/92 (Ranger II), B.M. Marriott, ed. Washington, D.C.: National Academy Press. IOM. 1994. Food Components to Enhance Performance, An Evaluation of Potential Peformance-Enhancing Food Components for Operational Rations, B.M. Marriott, ed. Washington, D.C.: National Academy Press. IOM. 1995. Not Eating Enough, Overcoming Underconsumption of Military Operational Rations, B.M. Marriott, ed. Washington, D.C.: National Academy Press. IOM. 1996. Nutritional Needs in Cold and in High-Altitude Environments, Applications for Military Personnel in Field Operations, B.M. Marriott and S.J. Carlson, eds. Washington, D.C.: National Academy Press. IOM. 1997. Dietary Reference Intakes: Calcium, Phosphorus, Magnesium, Vitamin D and Fluoride. Washington D.C.: National Academy Press. IOM. 1998. Assessing Readiness in Military Women: The Relationship of Body Composition, Nutrition, and Health. Washington, D.C.: National Academy Press. IOM. 1999. Military Strategies for Sustainment of Nutrition and Immune Function in the Field. Washington, D.C.: National Academy Press. Jacobi, C.A., J. Ordemann, F. Wenger, K. Zuckerman, H.D. Volk, and J.M. Muller. 1997. The influence of glutamine substitution in postoperative parenteral nutrition on immunologic function. First results of a prospective randomized trial (abstract). Shock 7(S):605. Jacobs, B.L. and C.A. Fornel. 1993.5-Hydroxytryptamine and motor control: a hypothesis. Trends in Neurosciences. 16:346-352. Jones, P.J.H., and I.K.K. Lee. 1996. Macronutrient requirements for work in cold environments. Pp. 189-202 in Nutritional Needs in Cold and in High-Altitude Environments: Applications for Military Personnel in Field Operations, B.M. Marriott and S.J. Carlson, eds. Institute of Medicine. Washington, D.C. : National Academy Press. Jorgensen, J.O.L., L. Thuesen, T. Ingemann-Hansen, S.A. Pedersen, J. Jorgensen, N.E. Skakkebaek, and J.S. Christiansen. 1989. Beneficial effects of growth hormone treatment in GH deficient adults. Lancet 1:1221-1225. Katz, A., S. Broberg, K. Sahlin, and J. Wahren. 1986. Muscle ammonia and amino acid metabolism during dynamic exercise in man. Clin. Physiol. 6:365-379. Kerr, G.R., E.S. Lee, M.M. Lan, R.J. Lorimor, E. Randall, R.N. Forthofer, M.A. Davis, and S.M. Magnetti. 1982. Relationships between dietary and biochemical measures of nutritional status in NHANES I data. Am. J. Clin. Nutr. 35:294-308. Kerstetter, J.E., and L.H. Allen. 1990. Dietary protein increases urinary calcium. J. Nutr. 120:134-136. King, N., K.E. Fridlund, and E.W. Askew. 1993. Nutrition issues of military women. J. Am. Coll. Nutr. 12:344-348. Kretsch, M.J., P.M. Confetti, and H.E. Sauberlich. 1986. Nutrient intake evaluation of male and female cadets at the United States Military Academy, West Point, New York, Report No. 218. Presidio of San Francisco, Calif. Letterman Army Institute of Research.

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Kishi, K., S. Miyatani, and G. Inoue. 1978. Requirements and utilization of egg protein by Japanese young men with marginal intakes of energy. J. Nutr. 108:658-669. King, N., J.E. Arsenault, S.H. Mutter, C.M. Champagne, T.C. Murphy, K.A. Westphal, and E.W. Askew. 1994. Nutritional intake of female soldiers during the U.S. Army basic combat training. Technical Report No. T94-17. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Kinney, J.M., and D.H. Elwyn. 1995. Amino acid metabolism in health and nutritional disease. Pp. 1-12 in Amino Acid Metabolism in Health and Nutritional Disease, L.A. Cynober, ed. Boca Raton, Fla.: CRC Press. Klicka, M.V., D.E. Sherman, N. King, K.E. Friedl, and E.W. Askew. 1993. Nutritional assessment of cadets at the U.S. Military Academy: Part 2. Assessment of nutritional intake. Technical Report T94-1. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Kreider, R.B., V. Miriel, and E. Bertum. 1993. Amino acid supplementation and exercise performance—Analysis of the proposed ergogenic value. Sports Med. 16:190-209. Kurzer, M.S. and D.H. Calloway. 1986. Effects of energy deprivation on sex hormone patterns in healthy menstruating women. Am. J. Physiol. 251:E483-E488. LeBlanc, J.A. 1996. Cold exposure, appetite, and energy balance. Pp. 203-214 in Nutritional Needs in Cold and in High-Altitude Environments: Applications for Military Personnel in Field Operations, B.M. Marriott and S.J. Carlson, eds. Institute of Medicine. Washington, D.C.: National Academy Press. Lehnert, H.R., D.K. Reinstein, and R.J. Wurtman. 1984a. Tyrosine reverses the depletion of brain norepinephrine and the behavioral deficits caused by tail-shock stress in rats. Pp. 81-91 in Stress: The Role of Catecholamines and Other Neurotransmitters, E. Usdin and R. Kvetnansky, eds. New York: Gordon and Beach. Lemon, P.R., M.A. Tarnopolsky, J.D. MacDougall, and S.A. Atkinson. 1992. Protein requirements and muscle mass/strength changes during intensive training in novice bodybuilders. J. Appl. Physiol. 73:767-775. Lieberman, H.R., 1994. Tyrosine and stress: Human and animal studies. Pp. 277-299 in Food Components to Enhance Performance, An Evaluation of Potential Performance—Enhancing Food Components for Operational Rations, B.M. Marriott, ed. Washington, D.C.: National Academy Press. Lieberman, H.R. and B. Shukitt-Hale. 1996. Food components and other treatments that may enhance performance at high altitude and in the cold. Pp. 453-465 in Nutritional Needs in Cold and in High Altitude Environments, B. Marriott and S. Newberry, eds. Washington, D.C.: National Academy Press. Lieberman, H.R., S. Corkin, B.J. Spring, J.H. Growdin, and R.J. Wurtman. 1983. Mood, performance, and pain sensitivity: Changes induced by food constituents. J. Psychiatr. Res. 17(2):135-145. Lieberman, H.R., S. Corkin, B.J. Spring, R.J. Wurtman, and J.H. Growdon. 1985. The effects of dietary neurotransmitter precursors on human behavior. Am. J. Clin. Nutr. 42:366-370. Lieberman, S.A., G.E. Butterfield, D. Harrison, and A.R. Hoffman. 1994. Anabolic effects of recombinant insulin-like growth factor-I in cachectic patients with the acquired immunodeficiency syndrome. J. Clin. Endocrinol. Metab. 78:404-410. Linkswiler, H.M., C.L. Joyce, and R. Anand. 1974. Calcium retention of young adult males as affected by level of protein and of calcium intake. Proc. N.Y. Acad. Sci. 36:333-340. Longenecker, J.B. 1961. Relationship between plasma amino acids and clinical chemistry of dogs. Pp. 469-485 in Progress in Meeting Protein Needs of Infants and Ire-school Children. Publ. 843. Washington, D.C.: National Academy of Sciences. Longenecker, J.B. 1963. Utilization of dietary protein. Pp. 113-144, Chapter 2, in Newer

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Methods of Nutritional Biochemistry, A.A. Albanese, ed. New York: Academic Press. Longenecker, J.B., and N.L. Hause. 1959. Relationship between plasma amino acids and composition of the ingested protein. Arch. Biochem. Biophys. 84:46-60. Longenecker, J.B., and N.L. Hause. 1961. Relationship between plasma amino acids and composition of the ingested protein. II. A shortened procedure to determine plasma amino acid (PAA) ratios. Am. J. Clin. Nutr. 9:356-363. Lukaski, H.C., J. Mendez, E.R. Buskirk, and S.H. Cohn. 1981. Relationship between endogenous 3-methylhistidine excretion and body composition. Am. J. Physiol. 240: E302-E307. Marchini, J.S., J. Cortiella, T. Hiramatsu, T.E. Chapman, and V.R. Young. 1993. Requirements for indispensable amino acids in adult humans: Longer term amino acid kinetic study with support for the adequacy of the Massachusetts Institute of Technology amino acid requirement pattern. Am. J. Clin. Nutr. 58:670-683. Matsueda, S., and Y. Niiyama. 1982. The effects of excess amino acids on maintenance of pregnancy and fetal growth in rats. J. Nutr. Sci. Vitaminol. (Tokyo). 28:557-573. McLarney, M.J., P.L. Pellett, and V.R. Young. 1996. Pattern of amino acid requirements in humans: An interspecies comparison using published amino acid requirements recommendations. J. Nutr. 126:1871-1882. Meredith, C.N., M.J. Zackin, W.R. Frontera, and W.J. Evans. 1989. Dietary protein requirements and body protein metabolism in endurance-trained men. J. Appl. Physiol. 66:2850-2856. Messing, R.B., and L.D. Lytle. 1977. Serotonin-containing neurons: their possible role in pain and analgesia. Pain 4:1-21. Millward, D.J. 1994. Can we define indispensable amino acid requirements and assess protein quality in adults? J. Nutr. 124:1509S-1516S. Millward, D.J., and J.P. Rivers. 1988. The nutritional role of indispensable amino acids and the metabolic basis for their requirements. Eur. J. Clin. Nutr. 42:367-393. Millward, D.J., and J.P. Rivers. 1989. The need for indispensable amino acids: The concept of the anabolic drive. Diab. Metab. Rev. 5(2):191-211. Millward, D.J., and J.C. Waterlow. 1996. Letter to the editor. Eur. J. Clin. Nutr. 50:832-833. Millward, D.J., J.L. Bowtell, P. Pacy, and M.J. Rennie. 1994. Physical activity, protein metabolism and protein requirements. Proc. Nutr. Soc. 53(1):223-240. Mitchell, H.H., and M. Edman. 1949. Nutrition and Resistance to Climatic Stress, with Reference to Man. Chicago, Ill.: Quartermaster Food and Container Institute for the Armed Forces. Mitchell, H.H., and M. Edman. 1951. Nutrition and Resistance to Climatic Stress, with Particular Reference to Man. Springfield, Ill.: Charles C. Thomas. Motil, K.J., C.M. Montandon, M. Thotathuchery, and C. Garza. 1990. Dietary protein and nitrogen balance in lactating and nonlactating women. Am. J. Clin. Nutr. 51:378-384. Motil, K.J., T.A. Davis, C.M. Montandon, W.W. Wong, and P.D. Klein. 1996. Whole-body protein turnover in the fed state is reduced in response to dietary protein restriction in lactating women. Am. J. Clin. Nutr. 64:32-39. Mulligan, K., and G.E. Butterfield. 1990. Discrepancies between energy intake and expenditure in physically active women. Br. J. Nutr. 64(1):23-36. Munro, H.N., and M.C. Crim. 1994. Protein and amino acids. In Modern Nutrition in Health and Disease, M.E. Shils, J.A. Olson, and M. Shike, eds. Philadelphia: Lea and Febiger. Neri, D.F., D. Wiegmann, R.R. Stanny, S.A. Shappell, A. McCardie, and D.L. McKay. 1995. The effects of tyrosine on cognitive performance during extended wakefulness. Aviat. Space Environ. Med. 66:313-319.

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Nindl, B.C., K.E. Friedl, P.N. Frykman, L.J. Marchitelli, R.L. Shippee, and J.F. Patton. 1997. Physical performance and metabolic recovery among lean, healthy men following a prolonged energy deficit. Int. J. Sports Med. 18:1-8. NRC (National Research Council). 1941. Recommended Dietary Allowances. Food and Nutrition Board. Washington, D.C.: National Academy Press. NRC. 1989. Recommended Dietary Allowances, 10th ed. Institute of Medicine. Washington, D.C.: National Academy Press. Nuñez, C., D. Gallagher, and S.B. Heymsfield. 1995. Appendicular skeletal muscle mass: Measurement with single frequency bioimpedance analysis. FASEB J. 9(4):A1012. Nuñez, C., D. Gallagher, M. Visser, F.X. Pi-Sunyer, Z. Wang, and S.B. Heymsfield. 1997. Bioimpedance analysis: Evaluation of leg-to-leg system based on pressure contact footpad electrodes. Med. Sci. Sports Exerc. 29:524-31. O'Riordain, M., K.C. Fearon, J.A. Ross, P. Rogers, J.S. Falconer, D.C. Bartolo, O.J. Garden, and D.C. Carter. 1994. Glutamine-supplemented parenteral nutrition enhances T-lymphocyte response in surgical patients undergoing colorectal resection. Ann Surg. 220:212-221. Owen, O.E., K.J. Smalley, D.A. D'Alessio, M.A. Mozzoli, E.K. Dawson. 1998. Protein, fat, and carbohydrate requirements during starvation: anaplerosis and cataplerosis. Am. J. Clin. Nutr. 68:12-34. Pardridge, W.M. 1977. Regulation of amino acid availability to the brain. Pp. 141-190 in Nutrition and the Brain, Vol. 1, R.J. Wurtman and J.J. Wurtman, eds. New York: Raven Press. Paul, G.L. 1989. Dietary protein requirements of physically active individuals. Sports Mad. 8:154-176. Pearlstone, D.B., R.F. Wolf, R.S. Berman, M. Burt, M.F. Brennan. 1994. Effect of systemic insulin on protein kinetics in postoperative cancer patients. Ann. Surg. Oncol. 1(4):321-332. Phillips, S.M., S.A. Atkinson, M.A. Tarnopolsky, and J.D. MacDougall. 1993. Gender differences in leucine kinetics and nitrogen balance in endurance athletes. J. Appl. Physiol. 75:2134-2141. Picou, D., and T. Taylor-Roberts. 1969. The measurement of total protein synthesis and catabolism and nitrogen turnover in infants in different nutritional states and receiving different amounts of dietary protein.. Clin. Sci. 36:283-296 Reeds, P.J., and P.R. Becket. 1996. Protein and amino acids. Pp. 67-86 in Present Knowledge in Nutrition, 7th ed., E.E. Ziegler and L.J. Filer, eds. Washington, D.C.: ILSI Press. Rennie, M.J. 1996. Influence of exercise on protein and amino acid metabolism. Pp. 995-1035 in American Physiological Society Handbook of Physiology on Exercise, Chapter 12, Section 12, Control of Energy Metabolism During Exercise, R. L. Terjung, ed. Bethesda, Md.: American Physiological Society. Robertson, W.G., P.J. Heyburn, M. Peacock, F.A. Hanes, and R. Swaminathan. 1979b. The effect of high animal protein intake on the risk of calcium-stone-formation in the urinary tract. Clin. Sci. 57:285-288. Rooyackers, O., and K.S. Nair. 1997. Hormonal regulation of human muscle protein metabolism. Ann. Rev. Nutr. 17:457-485. Rose, M.S. and D.E. Carlson. 1986. Effects of A Ration meals on body weight during sustained field operations. Technical Report T2-87. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Rose, M.S., P.C. Szlyk, R.P. Francesconi, L.S. Lester, L. Armstrong, W. Matthew, A.V. Cardello, R.D. Popper, I. Sils, G. Thomas, D. Schilling, and R. Whang. 1989. Effectiveness and acceptability of nutrient solutions in enhancing fluid intake in the

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance heat. Technical Report No. T10-89. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Rose, R.W., C.J. Baker, W. Wisnaskas, J.S.A. Edwards, and M.S. Rose. 1989. Dietary assessment of U.S. Army basic trainees at Fort Jackson, South Carolina. Technical Report No. T6-89. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Rowbottom, D.G., D. Keast, C. Goodman, and A.R. Morton 1995. The haernatological, biochemical and immunological profile of athletes suffering from the overtraining syndrome. Eur. J. Appl. Physiol. 70:502-509. Rush, D., Z. Stein, and M.A. Susser. 1980. A randomized controlled trial of prenatal nutritional supplementation in New York City. Pediatrics 65:653-697. Sahlin, K., A. Katz, and S. Broberg. 1990. Tricarboxylic acid cycle intermediates in human muscle during prolonged exercise. Am. J. Physiol. 159:C834-C841. Sahlin, K., L. Jorfeldt, and K.G. Henriksson. 1995. Tricarboxylic acid cycle intermediates during incremental exercise in healthy subjects and in patients with McArdle's disease. Clin. Sci. 19:687-693. Sakurai, Y., A. Aarsland, D.N. Herndon, D. L. Chinkes, E. Pierre, T.T. Nguyen, B.W. Patterson, and R.R. Wolfe. 1995. Stimulation of muscle protein synthesis by long-term insulin infusion in severely burned patients. Ann. Surg. 222(3):283-294. Schuette, S.A., and H.M. Linkswiler. 1982. Effects on Ca and P metabolism in humans by adding meat, meat plus milk, or purified proteins plus Ca and P to a low protein diet. J. Nutr. 112:338-349. Schwartz, R.S. 1995. Trophic factor supplementation: effect on the age-associated changes in body composition. J. Gerontol. A. Biol. Sci. Med. Sci. 50:151-156. Seltzer, S., D. Dewart, R. L. Pollack, and E. Jackson. 1983. The effects of dietary tryptophan on chronic maxillofacial pain and experimental pain tolerance. J. Psychiat. Res. 17(2):181-186. Shapses, S.A., S.P. Robins, E.I. Schwartz, and H. Chowdhury. 1995. Short-term changes in calcium but not protein intake alter the rate of bone resorption in healthy subjects as assessed by urinary pyridinium cross-link excretion. J. Nutr. 125:2814-2821. Sharp, T., S.R. Bramwell, and D.G. Grahame-Smith. 1992. Effect of acute administration of L-tryptophan on the release of 5-HT in rat hippocampus in relation to serotoninergic neuronal activity: An in vivo microdialysis study. Life Sci. 50:1215-1223. Shukitt-Hale, B., M.J. Stillman, and H.R. Lieberman. 1996. Tyrosine administration prevents hypoxia-induced decrements in learning and memory. Physiol. Behav. 59:867-871. Shurtleff, D., J.R. Thomas, S.T. Ahlers, and J. Schrot. 1993. Tyrosine ameliorates a cold-induced delayed matching-to-sample performance decrement in rats. Psychopharmacol. 112:228-232. Shurtleff, D., J.R. Thomas, J. Schrot, K. Kowalski, and R. Harford. 1994. Tyrosine reverses a cold-induced working memory deficit in humans. Pharmacol. Biochem. Behav. 47(4):935-941. Souba, W.W., and D.W. Wilmore. 1994. Diet and nutrition in the care of the patient with surgery, trauma, and sepsis. Pp. 1207-1240 in Modem Nutrition in Health and Disease, 8th e., M.E. Shils, J.A. Olson, and M. Shike, eds. Philadelphia: Lea and Febiger. Spencer, H., L. Kramer, and D. Osis. 1988. Do protein and phosphorus cause calcium loss? J. Nutr. 118:657-660. Stein, T.P., R.W. Hoyt, M.O. Toole, M.J. Leskiw, and M.D. Schluter. 1989. Protein and energy metabolism during prolonged exercise in trained athletes. Int. J. Sports Med. 10:311-316. Stone, E. A. 1975. Stress and catecholamines. Pp. 31-71 in Catecholamines and Behavior, A.J. Freidhoff, ed. New York: Plenum Press.

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Stroud, M.A., A.A. Jackson, and J.C. Waterlow. 1996. Protein turnover rates of two human subjects during an unassisted crossing of Antarctica. Br. J. Nutr. 16:165-174. Stucky, W.P., and A.E. Harper. 1962. Effects of altering indispensable to dispensable amino acids in diets for rats. J. Nutr. 78:278-286. Szeto, E.G., D.E. Carlson, T.B. Dugan, and J.C. Buchbinder. 1987. A comparison of nutrient intakes between a Ft. Riley contractor-operated and a Ft. Lewis military-operated garrison dining facility. Technical Report No. T2-88. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Szeto, E.G., T.B. Dugan, and J.A. Gallo. 1988. Assessment of habitual diners' nutrient intakes in a military-operated garrison dining facility, Ft. Devens I. Technical Report No. T3-89. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Szeto, E.G., J.A. Gallo, and K.W. Samonds. 1989. Passive nutrition intervention in a military-operated garrison dining facility, Ft. Devens II. Technical Report No. T7-89. Natick, Mass: U.S. Army Research Institute of Environmental Medicine. Tarnopolsky, M.A., J.D. Mac Dougal, and S.A. Atkinson. 1988. Influence of protein intake and training status on nitrogen balance and lean body mass. J. Appl. Physiol. 64:187-193. Tarnopolsky, M.A., P.W.R. Lemon, J.D. MacDougall, and J.A. Atkinson. 1990a. Effect of body building exercise on protein requirements. Can. J. Sport Sci. 15:225-226. Tarnopolsky, L.J., J.D. MacDougall, S.A. Atkinson, M.A. Tarnopolsky, and J.R. Sutton. 1990b. Gender differences in substrate for endurance exercise. J. Appl. Physiol. 68:302-308. Tarnopolsky, M.A., S.A. Atkinson, S.M. Phillips, and J.D. Mac Dougal. 1995. Carbohydrate loading and metabolism during exercise in men and women. J. Appl. Physiol. 78:1360-1368. Thomas, C.D., K.E. Friedl, M.Z. Mays, S.H. Mutter, and R.J. Moore. 1995. Nutrient intakes and nutritional status of soldiers consuming the Meal, Ready-to-Eat (MRE XII) during a 30-day field training exercise. Technical Report T95-6. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Tipton, K.D., and R.R. Wolfe. 1998. Exercise-induced changes in protein metabolism. Acta Physiol. Scand. 162(3): 377-387. Tobin, J., and D. Spector. 1986. Dietary protein has no effect on future creatinine clearance. Gerontologist 25:59A. Todd, K.S., G.E. Butterfield, and D.H. Calloway. 1984. Nitrogen balance in men with adequate and deficient energy intake at three levels of work. J. Nutr. 114:2107-2118. Tschope, W., and E. Ritz. 1985. Sulfur-containing amino acids are the major determinant of urinary calcium. Mineral Electrolyte Metab. 11:137-139. USACDEC/USARIEM (U.S. Army Combat Developments and Experimentation Center and U.S. Army Research Institute of Environmental Medicine). 1986. Combat Field Feeding System-Force Development Test and Experimentation (CFFS-FDTE) Technical Report CDEC-TR-85-006A . Vol. 1, Basic Report; vol. 2, Appendix A; vol. 3, Appendixes B through L. Fort Ord, Calif.: U.S. Army Combat Developments and Experimentation Center. U.S. Department of the Army. 1947. Army Regulation 40-250. Nutrition. Washington, D.C. Van der Hulst, R.R., B.K. van Kreel, M.F. von Meyenfeldt, R.J. Brummer, J.W. Arends, N.E. Deutz, and P.B. Soeters. 1993. Glutamine and the preservation of gut integrity. Lancet 341 (8957): 1363-1365. Walser, M. 1992. Dietary proteins and their relationship to kidney disease. Pp. 168-178 in Dietary Proteins in Health and Disease, G.U. Liepa, ed. Champaign, Ill.: American Oil Chemists' Society. Wang, Z., M. Visser, R. Ma, R. Baumgartner, D. Kotler, D. Gallagher, and S.B. Heymsfield.

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance 1996. Skeletal muscle mass: Evaluation of neutron activation and dual-energy x-ray absorptiometry methods. J. Appl. Physiol. 80(3):824-831. Wang, Z., P. Deurenberg, D.E. Matthews, and S.B. Heymsfield. 1998. Urinary 3-methylhistidine excretion: Association with total body skeletal muscle mass by computerized axial tomography. J. Parenter. Enteral Nutr. 22(2): 82-86. Warber, J.P., F.M. Kramer, S.M. McGraw, L.L. Lesher, W. Johnson, and A.D. Cline. 1996. The Army Food and Nutrition Survey, 1995-97. Technical Report. Natick, Mass.: U.S. Army Research Institute of Environmental Medicine. Walters, J.K., M. Davis, M.H. Sheard. 1979. Tryptophan-free diet: effects on the acoustic startle reflex in rats. Psychopharmacology (Berl) 62(2):103-109. Waterlow, J.C. 1996. The requirements of adult man for indispensable amine acids. Eur. J. Clin. Nutr. 50:S151-176. Welle, S., C. Thornton, M. Statt, and B. McHenry. 1996. Growth hormone increases muscle mass and strength but does not rejuvenate myofibrillar protein synthesis in healthy subjects over 60 years old. J. Clin. Endocrinol. Metab. 81:3239-3243. Wilmore, D.W. 1991. Catabolic illness: Strategies for enhancing recovery. N. Engl. J. Med. 325(10):695-702. Wilmore, D.W. 1997a. Glutamine saves lives! What does it mean? Nutrition 13(4):375-376. Wolf, R.F., D.B. Pearlstone, E. Newman, M.J. Heslin, A. Gonenne, M.E. Burt, and M.F. Brennan. 1992. Growth hormone and insulin reverse net whole body and skeletal muscle protein catabolism in cancer patients. Ann. Surg. 216:280-258. Wurtman, J.J., and J.D. Fernstrom. 1979. Free amine acid, protein and fat contents of breast milk from Guatemalan mothers consuming a corn-based diet. Early Human Development 3:67-77. Wurtman, R.J., F. Hefti, and E. Melamed. 1981. Precursor control of neurotransmitter synthesis. Pharmacol. Rev. 32:315-335. Yarasheski, K.E., J.J. Zachwieja, J.A. Campell, and D.M. Bier. 1995. Effect of growth hormone and resistance training on muscle growth and strength in older men. Am. J. Physiol. 268:E268-E276. Young, V.R. 1987. McCollum Award Lecture: Kinetics of human amine acid metabolism: Nutritional implications and some lessons. Am. J. Clin. Nutr. 46:709-725. Young, V.R. 1994. Adult amine acid requirement: The case for a major revision in current recommendations. J. Nutr. 124:1517S-1523S. Young, V.R., and A. E. El-Khoury. 1995a. Can amine acid requirements for nutritional maintenance in adult humans be approximated from the amine acid composition of body mixed proteins? Proc. Natl. Acad. Sci. 921:300-304. Young, V.R., and J.S. Marchini. 1990. Mechanisms and nutritional significance of metabolic responses to altered intakes of protein and amine acids, with reference to nutritional adaptation in humans. Am. J. Clin. Nutr. 51:270-289. Young, V.R., D.M. Bier, and P.L. Pellet. 1989. A theoretical basis for increasing current estimates of the amine acid requirements in adult man with experimental support. Am. J. Clin. Nutr. 50:80-92. Zawadzki, K.M., B.B. Yaspelkis, and J.L. Ivy. 1992. Carbohydrate-protein complex increases the rate of muscle glycogen storage after exercise. J. Appl. Physiol. 72:1854-1859. Zello, G.A., P.B. Pencharz, and R.O. Ball. 1993. Dietary lysine requirement of young adult males determined by oxidation of l-[l-13C]phenylalanine. Am. J. Physiol. 264:E677-E685. Zemel, M.B. 1988. Calcium utilization: Effect of varying level and source of dietary protein. Am. J. Clin Nutr. 48:880-883. Ziegler, T.R., L.S. Young, K. Benfell, M. Scheltinga, K. Hortos, R. Bye, F.D. Morrow, D.O.

OCR for page 19
The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Jacobs, R.J. Smith, J.H. Antin, and D.W. Wilmore. 1992. Clinical and metabolic efficacy of glutamine-supplemented parenteral nutrition after bone marrow transplantation. A randomized, double-blind, controlled study. Ann. Intern. Med. 116(10):821-828. Ziegler, T.R., R.L. Bye, R.L. Persinger, L.S. Young, J.H. Antin, and D.W. Wilmore. 1994. Glutamine-enriched parenteral nutrition increases circulating lymphocytes after bone marrow transplantation. J. Parenter. Enteral Nutr. 18:17S.

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